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Conserved domains on  [gi|193202555|ref|NP_001122450|]
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PH domain-containing protein [Caenorhabditis elegans]

Protein Classification

kinesin family protein; PEPP family PH domain-containing protein( domain architecture ID 12913599)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to carboxy-terminal kinesins that contains a C-terminal domain responsible for the motor activity (it hydrolyzes ATP and binds microtubules)| PEPP (phosphoinositol 3-phosphate-binding protein) family PH (pleckstrin homology) domain-containing protein similar to PH domain region of vertebrate pleckstrin homology domain-containing family A member 4/5/6/7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
13-154 5.23e-71

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269942  Cd Length: 136  Bit Score: 231.56  E-value: 5.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  13 NNGKCKICYKSKQNHSSESIENAKMNRKVTACGFLYVAPPNLDFSMQSHSAKRWQRRWFTLFDSGDLTYAIDNSMDTLPQ 92
Cdd:cd01236    1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193202555  93 LSIDMSLCYRVSEAHAITGNAHSILLAFNKTredqpsIIYIKADTTEEIRWWQNGLSKYANS 154
Cdd:cd01236   81 GSIDMSQCTEVTDAEARTGHPHSLAITTPER------IHFVKADSKEEIRWWLELLAVYPRT 136
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
292-394 2.41e-50

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270094  Cd Length: 104  Bit Score: 172.52  E-value: 2.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVYPSASARNYGIEIKCRRT-RYVLSAMT 370
Cdd:cd13275    1 KKGWLMKQGSRQGEWSKHWFVLRGAALKYYRDPSAEEAGELDGVIDLSSCTEVTELPVSRNYGFQVKTWDGkVYVLSAMT 80
                         90       100
                 ....*....|....*....|....
gi 193202555 371 PGIRDSWVSALQQNRHHPSPTFTE 394
Cdd:cd13275   81 SGIRTNWIQALRKAAGLPSPPALP 104
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
518-885 1.51e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   518 REEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDDSARRKRDAINQEIKELRITLKSSEDELHRYRKEVDTLRR 597
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   598 QISQNSQTVTLQRAVLSTLRTQLSALSSLLRSslflgAVDLFDSLDNILDRISVDL-NLEQTEDVLRKTAELFEKVSSAV 676
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQI-----LRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   677 TIPYLS-----DSWTMTEPEKEPRERTPEDVVEETIREIR---------RNHTSEVESIKSQCEQRLAVLKERAEREEGR 742
Cdd:TIGR02168  350 KEELESleaelEELEAELEELESRLEELEEQLETLRSKVAqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKK 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   743 RKKLQEQLV-MASTRSDESISSVKTSFSQmLAEQRKTFDEELDCVKKEHEERLMEEKHA-TRL-ALEAVRRAHEEELKNV 819
Cdd:TIGR02168  430 LEEAELKELqAELEELEEELEELQEELER-LEEALEELREELEEAEQALDAAERELAQLqARLdSLERLQENLEGFSEGV 508
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193202555   820 AE--KNKTGEGNHIGRQSeifdemreELINVCALYSAkCLENSqLDEQLSNLISEKEASVELSIENDK 885
Cdd:TIGR02168  509 KAllKNQSGLSGILGVLS--------ELISVDEGYEA-AIEAA-LGGRLQAVVVENLNAAKKAIAFLK 566
 
Name Accession Description Interval E-value
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
13-154 5.23e-71

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269942  Cd Length: 136  Bit Score: 231.56  E-value: 5.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  13 NNGKCKICYKSKQNHSSESIENAKMNRKVTACGFLYVAPPNLDFSMQSHSAKRWQRRWFTLFDSGDLTYAIDNSMDTLPQ 92
Cdd:cd01236    1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193202555  93 LSIDMSLCYRVSEAHAITGNAHSILLAFNKTredqpsIIYIKADTTEEIRWWQNGLSKYANS 154
Cdd:cd01236   81 GSIDMSQCTEVTDAEARTGHPHSLAITTPER------IHFVKADSKEEIRWWLELLAVYPRT 136
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
292-394 2.41e-50

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270094  Cd Length: 104  Bit Score: 172.52  E-value: 2.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVYPSASARNYGIEIKCRRT-RYVLSAMT 370
Cdd:cd13275    1 KKGWLMKQGSRQGEWSKHWFVLRGAALKYYRDPSAEEAGELDGVIDLSSCTEVTELPVSRNYGFQVKTWDGkVYVLSAMT 80
                         90       100
                 ....*....|....*....|....
gi 193202555 371 PGIRDSWVSALQQNRHHPSPTFTE 394
Cdd:cd13275   81 SGIRTNWIQALRKAAGLPSPPALP 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
290-383 8.58e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 65.26  E-value: 8.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   290 TLRKGWLMLRGKSDND-WCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVY---PSASARNYGIEIKCR-RTRY 364
Cdd:smart00233   1 VIKEGWLYKKSGGGKKsWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREapdPDSSKKPHCFEIKTSdRKTL 80
                           90
                   ....*....|....*....
gi 193202555   365 VLSAMTPGIRDSWVSALQQ 383
Cdd:smart00233  81 LLQAESEEEREKWVEALRK 99
PH pfam00169
PH domain; PH stands for pleckstrin homology.
292-383 5.36e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.49  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  292 RKGWLMLRGKSDND-WCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVYPSASA---RNYGIEIK----CRRTR 363
Cdd:pfam00169   3 KEGWLLKKGGGKKKsWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFELRtgerTGKRT 82
                          90       100
                  ....*....|....*....|
gi 193202555  364 YVLSAMTPGIRDSWVSALQQ 383
Cdd:pfam00169  83 YLLQAESEEERKDWIKAIQS 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
518-885 1.51e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   518 REEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDDSARRKRDAINQEIKELRITLKSSEDELHRYRKEVDTLRR 597
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   598 QISQNSQTVTLQRAVLSTLRTQLSALSSLLRSslflgAVDLFDSLDNILDRISVDL-NLEQTEDVLRKTAELFEKVSSAV 676
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQI-----LRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   677 TIPYLS-----DSWTMTEPEKEPRERTPEDVVEETIREIR---------RNHTSEVESIKSQCEQRLAVLKERAEREEGR 742
Cdd:TIGR02168  350 KEELESleaelEELEAELEELESRLEELEEQLETLRSKVAqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKK 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   743 RKKLQEQLV-MASTRSDESISSVKTSFSQmLAEQRKTFDEELDCVKKEHEERLMEEKHA-TRL-ALEAVRRAHEEELKNV 819
Cdd:TIGR02168  430 LEEAELKELqAELEELEEELEELQEELER-LEEALEELREELEEAEQALDAAERELAQLqARLdSLERLQENLEGFSEGV 508
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193202555   820 AE--KNKTGEGNHIGRQSeifdemreELINVCALYSAkCLENSqLDEQLSNLISEKEASVELSIENDK 885
Cdd:TIGR02168  509 KAllKNQSGLSGILGVLS--------ELISVDEGYEA-AIEAA-LGGRLQAVVVENLNAAKKAIAFLK 566
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
513-897 1.30e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 513 QEKPSR-EEIQRQIgtaSRISSDETRLRSLEQQVDNLRTQLDAAKDDSARRKRDAINQ---EIKELRITLKSSEDELHRY 588
Cdd:COG4717  142 AELPERlEELEERL---EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDlaeELEELQQRLAELEEELEEA 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 589 RKEVDTLRRQISQNSQTVTLQRavlstlrtqlsalssllrsslflgAVDLFDSLDNILDRISVDLNLEQTEDVLRKTAEL 668
Cdd:COG4717  219 QEELEELEEELEQLENELEAAA------------------------LEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 669 FEKVsSAVTIPYLSDSWTMTEPEKEPRERTPEDVveETIREIRRNHTSEVESIKSQCEQRLAVLKERAEREEGRRKKLQE 748
Cdd:COG4717  275 IAGV-LFLVLGLLALLFLLLAREKASLGKEAEEL--QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 749 QLVMASTRSDE-SISSVKTSFSQMLAEQRKTFDEELD--CVKKEHEERLMEEKHATRLALEAVRRAHEEELKNVAEKNKT 825
Cdd:COG4717  352 LLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRaaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193202555 826 GEGNHIGRQSEIFDEMREELINVCAlysakclensQLDEQLSNLISEKEASvELSIENDKLRSEIDRKSKEI 897
Cdd:COG4717  432 EELEELEEELEELEEELEELREELA----------ELEAELEQLEEDGELA-ELLQELEELKAELRELAEEW 492
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
44-150 8.91e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 42.54  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555    44 CGFLYVappnldfsMQSHSAKRWQRRWFTLFDSGdLTYAIDNS--MDTLPQLSIDMSLCyRVSEAHAIT--GNAHSILLa 119
Cdd:smart00233   4 EGWLYK--------KSGGGKKSWKKRYFVLFNST-LLYYKSKKdkKSYKPKGSIDLSGC-TVREAPDPDssKKPHCFEI- 72
                           90       100       110
                   ....*....|....*....|....*....|.
gi 193202555   120 fnktREDQPSIIYIKADTTEEIRWWQNGLSK 150
Cdd:smart00233  73 ----KTSDRKTLLLQAESEEEREKWVEALRK 99
PH pfam00169
PH domain; PH stands for pleckstrin homology.
60-144 5.65e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.24  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   60 SHSAKRWQRRWFTLFDSGDLTYAIDNSM-DTLPQLSIDMSLCYRVS-EAHAITGNAHSILLAFNKTREDQPsiIYIKADT 137
Cdd:pfam00169  12 GGKKKSWKKRYFVLFDGSLLYYKDDKSGkSKEPKGSISLSGCEVVEvVASDSPKRKFCFELRTGERTGKRT--YLLQAES 89

                  ....*..
gi 193202555  138 TEEIRWW 144
Cdd:pfam00169  90 EEERKDW 96
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
519-920 1.59e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   519 EEIQRQIGTASRISSDETRLRS-LEQQVDNLRTQLDAAKDDSARRKRDAiNQEIKELRITLKSSEDELHRYRKEV----D 593
Cdd:pfam15921  120 QEMQMERDAMADIRRRESQSQEdLRNQLQNTVHELEAAKCLKEDMLEDS-NTQIEQLRKMMLSHEGVLQEIRSILvdfeE 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   594 TLRRQISQNSQTVTLQRAVLSTLRTQLSALSSLLRSSLFLGAVDLFDSLDNIL--DRISVDLNLEQTEDVLRKTAELFEK 671
Cdd:pfam15921  199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKseSQNKIELLLQQHQDRIEQLISEHEV 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   672 VSSAVTipylsdswtmtepEKEPRERTPEDVVE---ETIREIRRN-------HTSEVESIKSQCEQRLavlKERAEREEG 741
Cdd:pfam15921  279 EITGLT-------------EKASSARSQANSIQsqlEIIQEQARNqnsmymrQLSDLESTVSQLRSEL---REAKRMYED 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   742 RRKKLQEQLVMASTRSDESISSvKTSFSQ-----------MLAEQRKTfDEELDcVKKEHEERLMEEKHATRLALEAVRR 810
Cdd:pfam15921  343 KIEELEKQLVLANSELTEARTE-RDQFSQesgnlddqlqkLLADLHKR-EKELS-LEKEQNKRLWDRDTGNSITIDHLRR 419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   811 -------------------------AHEEELKNVAEKNKTGEgnHIGRQSEIFDEMREELINVCALYSAK--CLENSQLD 863
Cdd:pfam15921  420 elddrnmevqrleallkamksecqgQMERQMAAIQGKNESLE--KVSSLTAQLESTKEMLRKVVEELTAKkmTLESSERT 497
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 193202555   864 -EQLSNLISEKEASVELS-IENDKLRSEIDRKSKEigdLQRKMNNYEKLSQSRTDPEVL 920
Cdd:pfam15921  498 vSDLTASLQEKERAIEATnAEITKLRSRVDLKLQE---LQHLKNEGDHLRNVQTECEAL 553
PRK11281 PRK11281
mechanosensitive channel MscK;
509-616 3.57e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  509 AASHQEKPSREEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDdsARRKRDAINQEIKELRITLKSSEDELHRY 588
Cdd:PRK11281   29 AASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDR--QKEETEQLKQQLAQAPAKLRQAQAELEAL 106
                          90       100
                  ....*....|....*....|....*...
gi 193202555  589 RKEVDTLRRQISQNSQTVTLQRAVLSTL 616
Cdd:PRK11281  107 KDDNDEETRETLSTLSLRQLESRLAQTL 134
 
Name Accession Description Interval E-value
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
13-154 5.23e-71

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269942  Cd Length: 136  Bit Score: 231.56  E-value: 5.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  13 NNGKCKICYKSKQNHSSESIENAKMNRKVTACGFLYVAPPNLDFSMQSHSAKRWQRRWFTLFDSGDLTYAIDNSMDTLPQ 92
Cdd:cd01236    1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193202555  93 LSIDMSLCYRVSEAHAITGNAHSILLAFNKTredqpsIIYIKADTTEEIRWWQNGLSKYANS 154
Cdd:cd01236   81 GSIDMSQCTEVTDAEARTGHPHSLAITTPER------IHFVKADSKEEIRWWLELLAVYPRT 136
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
292-394 2.41e-50

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270094  Cd Length: 104  Bit Score: 172.52  E-value: 2.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVYPSASARNYGIEIKCRRT-RYVLSAMT 370
Cdd:cd13275    1 KKGWLMKQGSRQGEWSKHWFVLRGAALKYYRDPSAEEAGELDGVIDLSSCTEVTELPVSRNYGFQVKTWDGkVYVLSAMT 80
                         90       100
                 ....*....|....*....|....
gi 193202555 371 PGIRDSWVSALQQNRHHPSPTFTE 394
Cdd:cd13275   81 SGIRTNWIQALRKAAGLPSPPALP 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
290-383 8.58e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 65.26  E-value: 8.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   290 TLRKGWLMLRGKSDND-WCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVY---PSASARNYGIEIKCR-RTRY 364
Cdd:smart00233   1 VIKEGWLYKKSGGGKKsWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREapdPDSSKKPHCFEIKTSdRKTL 80
                           90
                   ....*....|....*....
gi 193202555   365 VLSAMTPGIRDSWVSALQQ 383
Cdd:smart00233  81 LLQAESEEEREKWVEALRK 99
PH pfam00169
PH domain; PH stands for pleckstrin homology.
292-383 5.36e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.49  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  292 RKGWLMLRGKSDND-WCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVYPSASA---RNYGIEIK----CRRTR 363
Cdd:pfam00169   3 KEGWLLKKGGGKKKsWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFELRtgerTGKRT 82
                          90       100
                  ....*....|....*....|
gi 193202555  364 YVLSAMTPGIRDSWVSALQQ 383
Cdd:pfam00169  83 YLLQAESEEERKDWIKAIQS 102
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
289-382 8.51e-09

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275402  Cd Length: 116  Bit Score: 54.16  E-value: 8.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 289 HTLRKGWLMLRGKSDNDWCKHWVVLAGLQLKLYkdvwaEDSTE---PLLTVDLSQCENVYPSASA----RNYGIEIKCRr 361
Cdd:cd13215   20 AVIKSGYLSKRSKRTLRYTRYWFVLKGDTLSWY-----NSSTDlyfPAGTIDLRYATSIELSKSNgeatTSFKIVTNSR- 93
                         90       100
                 ....*....|....*....|.
gi 193202555 362 tRYVLSAMTPGIRDSWVSALQ 382
Cdd:cd13215   94 -TYKFKADSETSADEWVKALK 113
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
292-381 2.25e-08

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 52.54  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLMLRGKSDND-WCKHWVVLAGLQLKLYKDVwAEDSTEPLLTVDLSQCENVYPSAS-ARNYGIEIKCRRTR-YVLSA 368
Cdd:cd00821    1 KEGYLLKRGGGGLKsWKKRWFVLFEGVLLYYKSK-KDSSYKPKGSIPLSGILEVEEVSPkERPHCFELVTPDGRtYYLQA 79
                         90
                 ....*....|...
gi 193202555 369 MTPGIRDSWVSAL 381
Cdd:cd00821   80 DSEEERQEWLKAL 92
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
518-885 1.51e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   518 REEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDDSARRKRDAINQEIKELRITLKSSEDELHRYRKEVDTLRR 597
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   598 QISQNSQTVTLQRAVLSTLRTQLSALSSLLRSslflgAVDLFDSLDNILDRISVDL-NLEQTEDVLRKTAELFEKVSSAV 676
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQI-----LRERLANLERQLEELEAQLeELESKLDELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   677 TIPYLS-----DSWTMTEPEKEPRERTPEDVVEETIREIR---------RNHTSEVESIKSQCEQRLAVLKERAEREEGR 742
Cdd:TIGR02168  350 KEELESleaelEELEAELEELESRLEELEEQLETLRSKVAqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKK 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   743 RKKLQEQLV-MASTRSDESISSVKTSFSQmLAEQRKTFDEELDCVKKEHEERLMEEKHA-TRL-ALEAVRRAHEEELKNV 819
Cdd:TIGR02168  430 LEEAELKELqAELEELEEELEELQEELER-LEEALEELREELEEAEQALDAAERELAQLqARLdSLERLQENLEGFSEGV 508
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193202555   820 AE--KNKTGEGNHIGRQSeifdemreELINVCALYSAkCLENSqLDEQLSNLISEKEASVELSIENDK 885
Cdd:TIGR02168  509 KAllKNQSGLSGILGVLS--------ELISVDEGYEA-AIEAA-LGGRLQAVVVENLNAAKKAIAFLK 566
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
64-144 3.36e-06

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 46.38  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  64 KRWQRRWFTLFDSGDLTYAIDNSMDTLPQLSIDMSLCYRVSEAHAITGNaHSILLAFNKTRedqpsIIYIKADTTEEIRW 143
Cdd:cd00821   14 KSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIPLSGILEVEEVSPKERP-HCFELVTPDGR-----TYYLQADSEEERQE 87

                 .
gi 193202555 144 W 144
Cdd:cd00821   88 W 88
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
285-385 1.13e-05

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270075  Cd Length: 110  Bit Score: 45.10  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 285 MSNVHTLRKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDVwAEDSTEPLLTV-DLSQCENVYPSASARNYGIeIKCRRTR 363
Cdd:cd13255    1 MISEAVLKAGYLEKKGERRKTWKKRWFVLRPTKLAYYKND-KEYRLLRLIDLtDIHTCTEVQLKKHDNTFGI-VTPARTF 78
                         90       100
                 ....*....|....*....|..
gi 193202555 364 YVlSAMTPGIRDSWVSALQQNR 385
Cdd:cd13255   79 YV-QADSKAEMESWISAINLAR 99
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
513-897 1.30e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 513 QEKPSR-EEIQRQIgtaSRISSDETRLRSLEQQVDNLRTQLDAAKDDSARRKRDAINQ---EIKELRITLKSSEDELHRY 588
Cdd:COG4717  142 AELPERlEELEERL---EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDlaeELEELQQRLAELEEELEEA 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 589 RKEVDTLRRQISQNSQTVTLQRavlstlrtqlsalssllrsslflgAVDLFDSLDNILDRISVDLNLEQTEDVLRKTAEL 668
Cdd:COG4717  219 QEELEELEEELEQLENELEAAA------------------------LEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 669 FEKVsSAVTIPYLSDSWTMTEPEKEPRERTPEDVveETIREIRRNHTSEVESIKSQCEQRLAVLKERAEREEGRRKKLQE 748
Cdd:COG4717  275 IAGV-LFLVLGLLALLFLLLAREKASLGKEAEEL--QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 749 QLVMASTRSDE-SISSVKTSFSQMLAEQRKTFDEELD--CVKKEHEERLMEEKHATRLALEAVRRAHEEELKNVAEKNKT 825
Cdd:COG4717  352 LLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRaaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193202555 826 GEGNHIGRQSEIFDEMREELINVCAlysakclensQLDEQLSNLISEKEASvELSIENDKLRSEIDRKSKEI 897
Cdd:COG4717  432 EELEELEEELEELEEELEELREELA----------ELEAELEQLEEDGELA-ELLQELEELKAELRELAEEW 492
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
291-381 1.84e-05

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270083  Cd Length: 114  Bit Score: 44.68  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 291 LRKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDvwaEDSTEPLLTVDLSQCE-NVYPSA--SARNYGIEI-------KCR 360
Cdd:cd13263    4 IKSGWLKKQGSIVKNWQQRWFVLRGDQLYYYKD---EDDTKPQGTIPLPGNKvKEVPFNpeEPGKFLFEIipggggdRMT 80
                         90       100
                 ....*....|....*....|...
gi 193202555 361 RTR--YVLSAMTPGIRDSWVSAL 381
Cdd:cd13263   81 SNHdsYLLMANSQAEMEEWVKVI 103
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
292-381 2.59e-05

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 44.23  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDVWAEDSTEPLLTVDLSQCENVYPS--ASARNYGIEIKCRRTRYVLSAM 369
Cdd:cd13276    1 KAGWLEKQGEFIKTWRRRWFVLKQGKLFWFKEPDVTPYSKPRGVIDLSKCLTVKSAedATNKENAFELSTPEETFYFIAD 80
                         90
                 ....*....|..
gi 193202555 370 TPGIRDSWVSAL 381
Cdd:cd13276   81 NEKEKEEWIGAI 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
44-150 8.91e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 42.54  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555    44 CGFLYVappnldfsMQSHSAKRWQRRWFTLFDSGdLTYAIDNS--MDTLPQLSIDMSLCyRVSEAHAIT--GNAHSILLa 119
Cdd:smart00233   4 EGWLYK--------KSGGGKKSWKKRYFVLFNST-LLYYKSKKdkKSYKPKGSIDLSGC-TVREAPDPDssKKPHCFEI- 72
                           90       100       110
                   ....*....|....*....|....*....|.
gi 193202555   120 fnktREDQPSIIYIKADTTEEIRWWQNGLSK 150
Cdd:smart00233  73 ----KTSDRKTLLLQAESEEEREKWVEALRK 99
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
507-610 1.64e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 507 SSAASHQEKPSREEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKD--DSARRKRDAINQEIKELRITLKSSEDE 584
Cdd:COG4942   12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKE 91
                         90       100
                 ....*....|....*....|....*.
gi 193202555 585 LHRYRKEVDTLRRQISQnsQTVTLQR 610
Cdd:COG4942   92 IAELRAELEAQKEELAE--LLRALYR 115
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
292-383 2.72e-04

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 40.74  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLM-LRGKSDNdWCKHWVVLAGLQLKLYKDVwAEDSTEPLLTVDL-SQCEnVYPSASARNygIEIKCRRTRYVLSAM 369
Cdd:cd13282    1 KAGYLTkLGGKVKT-WKRRWFVLKNGELFYYKSP-NDVIRKPQGQIALdGSCE-IARAEGAQT--FEIVTEKRTYYLTAD 75
                         90
                 ....*....|....
gi 193202555 370 TPGIRDSWVSALQQ 383
Cdd:cd13282   76 SENDLDEWIRVIQN 89
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
518-922 4.29e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 518 REEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDDSARRKRDAINQEIKELRITLKSSEDELHRYRKEVDTLRR 597
Cdd:COG1196  195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 598 QISQNSQTVTLQRAVLSTLRTQLSALSSllrsslflgavdlfdsldnildriSVDLNLEQTEDVLRKTAELfekvssavt 677
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQ------------------------DIARLEERRRELEERLEEL--------- 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 678 ipylsdswtmtepekeprertpedvvEETIREIRRNHTSEVESIKSQcEQRLAVLKERAEREEGRRKKLQEQLVMASTRS 757
Cdd:COG1196  322 --------------------------EEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 758 DESISSVKTSFSQMLAEQRKTFDEELdcvKKEHEERLMEEKHATRLALEAVRRAHEEELKNVAEKnktgegnhIGRQSEI 837
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAA---QLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEA 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 838 FDEMREELinvcalysakcLENSQLDEQLSNLISEKEASVELSIEN-DKLRSEIDRKSKEIGDLQRKMNNYEKLSQSRTD 916
Cdd:COG1196  444 LEEAAEEE-----------AELEEEEEALLELLAELLEEAALLEAAlAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512

                 ....*.
gi 193202555 917 PEVLAG 922
Cdd:COG1196  513 ALLLAG 518
PH pfam00169
PH domain; PH stands for pleckstrin homology.
60-144 5.65e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.24  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   60 SHSAKRWQRRWFTLFDSGDLTYAIDNSM-DTLPQLSIDMSLCYRVS-EAHAITGNAHSILLAFNKTREDQPsiIYIKADT 137
Cdd:pfam00169  12 GGKKKSWKKRYFVLFDGSLLYYKDDKSGkSKEPKGSISLSGCEVVEvVASDSPKRKFCFELRTGERTGKRT--YLLQAES 89

                  ....*..
gi 193202555  138 TEEIRWW 144
Cdd:pfam00169  90 EEERKDW 96
PH_RhoGap24 cd13379
Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ...
290-338 6.26e-04

Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241530  Cd Length: 114  Bit Score: 40.34  E-value: 6.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 193202555 290 TLRKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDvwaEDSTEPLLTVDL 338
Cdd:cd13379    3 VIKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKD---EDETKPLGTIFL 48
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
489-677 7.98e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  489 VARVKERRADIRQRH--ASNSSAASHQEKPSREEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDDSArrkrda 566
Cdd:COG4913   612 LAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD------ 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  567 inqEIKELRITLKSSEDELHRYRKEVDTLRRQISQNSQTVTLQRAVLSTLRTQLSALSSLLRSSLFLGAVDLFDSL--DN 644
Cdd:COG4913   686 ---DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlgDA 762
                         170       180       190
                  ....*....|....*....|....*....|...
gi 193202555  645 ILDRISVDLNlEQTEDVLRKTAELFEKVSSAVT 677
Cdd:COG4913   763 VERELRENLE-ERIDALRARLNRAEEELERAMR 794
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
494-611 8.12e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 494 ERRADIRQRHASNSSAASHQEKPSREEIQRQIGTASRISSDETRLRSLEQQvdnLRTQLDAAKDDSARRKRDAINQEIKE 573
Cdd:COG4717  360 EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ---LEELLGELEELLEALDEEELEEELEE 436
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 193202555 574 LRITLKSSEDELHRYRKEVDTLRRQISQNSQTVTLQRA 611
Cdd:COG4717  437 LEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
293-381 1.34e-03

Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270111  Cd Length: 102  Bit Score: 39.15  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 293 KGWL-MLRGKSDNDWCKHWVVLAGLQLKLYKDvwaEDSTEPLLTVDLSQCENVY---PSASARNYGIEIKCRRTRYVLSA 368
Cdd:cd13299    9 QGYLqVLKKKGVNQWKKYWLVLRNRSLSFYKD---QSEYSPVKIIPIDDIIDVVeldPLSKSKKWCLQIITPEKRIRFCA 85
                         90
                 ....*....|...
gi 193202555 369 MTPGIRDSWVSAL 381
Cdd:cd13299   86 DDEESLIKWLGAL 98
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
305-383 1.47e-03

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 39.57  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 305 DWCKHWVVLAGLQLKlykdVWA----EDSTEPLLTVDLSQCEN------------------VYPSASARNYGIEIKCRRT 362
Cdd:cd01263   19 AWHRRWCVLRGGYLS----FWKypddEEKKKPIGSIDLTKCITekvepaprelcarpntflLETLRPAEDDDRDDTNEKI 94
                         90       100
                 ....*....|....*....|.
gi 193202555 363 RYVLSAMTPGIRDSWVSALQQ 383
Cdd:cd01263   95 RVLLSADTKEERIEWLSALNQ 115
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
519-920 1.59e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   519 EEIQRQIGTASRISSDETRLRS-LEQQVDNLRTQLDAAKDDSARRKRDAiNQEIKELRITLKSSEDELHRYRKEV----D 593
Cdd:pfam15921  120 QEMQMERDAMADIRRRESQSQEdLRNQLQNTVHELEAAKCLKEDMLEDS-NTQIEQLRKMMLSHEGVLQEIRSILvdfeE 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   594 TLRRQISQNSQTVTLQRAVLSTLRTQLSALSSLLRSSLFLGAVDLFDSLDNIL--DRISVDLNLEQTEDVLRKTAELFEK 671
Cdd:pfam15921  199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKseSQNKIELLLQQHQDRIEQLISEHEV 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   672 VSSAVTipylsdswtmtepEKEPRERTPEDVVE---ETIREIRRN-------HTSEVESIKSQCEQRLavlKERAEREEG 741
Cdd:pfam15921  279 EITGLT-------------EKASSARSQANSIQsqlEIIQEQARNqnsmymrQLSDLESTVSQLRSEL---REAKRMYED 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   742 RRKKLQEQLVMASTRSDESISSvKTSFSQ-----------MLAEQRKTfDEELDcVKKEHEERLMEEKHATRLALEAVRR 810
Cdd:pfam15921  343 KIEELEKQLVLANSELTEARTE-RDQFSQesgnlddqlqkLLADLHKR-EKELS-LEKEQNKRLWDRDTGNSITIDHLRR 419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555   811 -------------------------AHEEELKNVAEKNKTGEgnHIGRQSEIFDEMREELINVCALYSAK--CLENSQLD 863
Cdd:pfam15921  420 elddrnmevqrleallkamksecqgQMERQMAAIQGKNESLE--KVSSLTAQLESTKEMLRKVVEELTAKkmTLESSERT 497
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 193202555   864 -EQLSNLISEKEASVELS-IENDKLRSEIDRKSKEigdLQRKMNNYEKLSQSRTDPEVL 920
Cdd:pfam15921  498 vSDLTASLQEKERAIEATnAEITKLRSRVDLKLQE---LQHLKNEGDHLRNVQTECEAL 553
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
490-619 2.73e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 490 ARVKERRADIRQRHASNSSAASHQEKpSREEIQRQIGTASR--------ISSDETRLRSLEQQVDNLRTQLDAAKDDSAR 561
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLK-QLAALERRIAALARriraleqeLAALEAELAELEKEIAELRAELEAQKEELAE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 562 RKR------------------------------DAINQEIKELRITLKSSEDELHRYRKEVDTLRRQISQNSQTVTLQRA 611
Cdd:COG4942  109 LLRalyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                 ....*...
gi 193202555 612 VLSTLRTQ 619
Cdd:COG4942  189 ALEALKAE 196
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
291-383 3.02e-03

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270073  Cd Length: 94  Bit Score: 37.75  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 291 LRKGWLMLRGKSDND--WCKHWVVLAGLQLKLYKdvwAEDSTEPLLTVDLSQCENVYPSASARnygIEIKCRRTRYVLSA 368
Cdd:cd13253    1 IKSGYLDKQGGQGNNkgFQKRWVVFDGLSLRYFD---SEKDAYSKRIIPLSAISTVRAVGDNK---FELVTTNRTFVFRA 74
                         90
                 ....*....|....*
gi 193202555 369 MTPGIRDSWVSALQQ 383
Cdd:cd13253   75 ESDDERNLWCSTLQA 89
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
292-382 3.44e-03

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270070  Cd Length: 98  Bit Score: 37.97  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 292 RKGWLMLR-GKSDNDWCKHWVVLAGLQLKLYKDVWAEDSTepLLTVDLSQCeNVYPSASA-RNYGIEIKCRRTRYVLSAM 369
Cdd:cd13250    1 KEGYLFKRsSNAFKTWKRRWFSLQNGQLYYQKRDKKDEPT--VMVEDLRLC-TVKPTEDSdRRFCFEVISPTKSYMLQAE 77
                         90
                 ....*....|...
gi 193202555 370 TPGIRDSWVSALQ 382
Cdd:cd13250   78 SEEDRQAWIQAIQ 90
PRK11281 PRK11281
mechanosensitive channel MscK;
509-616 3.57e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  509 AASHQEKPSREEIQRQIGTASRISSDETRLRSLEQQVDNLRTQLDAAKDdsARRKRDAINQEIKELRITLKSSEDELHRY 588
Cdd:PRK11281   29 AASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDR--QKEETEQLKQQLAQAPAKLRQAQAELEAL 106
                          90       100
                  ....*....|....*....|....*...
gi 193202555  589 RKEVDTLRRQISQNSQTVTLQRAVLSTL 616
Cdd:PRK11281  107 KDDNDEETRETLSTLSLRQLESRLAQTL 134
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
288-382 5.18e-03

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 37.30  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 288 VHTLRKGWLMLRGKSDNDWCKHWVVLAGLQLKLYKDvwaEDSTEPLLTVDLSQCENV-YPSASARNYGIEIKCRRTRYVL 366
Cdd:cd10573    1 SLGSKEGYLTKLGGIVKNWKTRWFVLRRNELKYFKT---RGDTKPIRVLDLRECSSVqRDYSQGKVNCFCLVFPERTFYM 77
                         90
                 ....*....|....*.
gi 193202555 367 SAMTPGIRDSWVSALQ 382
Cdd:cd10573   78 YANTEEEADEWVKLLK 93
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
529-601 5.84e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 529 SRISSDETRLRSLEQQVDNLRTQLDAAKD---------DSARRKRDAINQEIKELRITLK---------SSEDELHRYRK 590
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEArleaaktelEDLEKEIKRLELEIEEVEARIKkyeeqlgnvRNNKEYEALQK 96
                         90
                 ....*....|.
gi 193202555 591 EVDTLRRQISQ 601
Cdd:COG1579   97 EIESLKRRISD 107
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
491-585 7.75e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555 491 RVKERRADIRQRHASNSSAASHQEKpSREEIQRQIGTA-SRISSDETRLRSLEQQVDNLRTQLDAAKD--DSARRKRDAI 567
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELES-ELEEAREAVEDRrEEIEELEEEIEELRERFGDAPVDLGNAEDflEELREERDEL 424
                         90
                 ....*....|....*...
gi 193202555 568 NQEIKELRITLKSSEDEL 585
Cdd:PRK02224 425 REREAELEATLRTARERV 442
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
487-619 9.81e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 9.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202555  487 SPVARVKERRADIRQRHASNSSAASHQEkpsREEIQRQIGTA-SRISSDETRLRSLEQQVDNLRTQLDAAKD--DSARRK 563
Cdd:COG4913   255 EPIRELAERYAAARERLAELEYLRAALR---LWFAQRRLELLeAELEELRAELARLEAELERLEARLDALREelDELEAQ 331
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193202555  564 R--------DAINQEIKELRITLKSSEDELHRYRKEVDTLRRQISQNSQTVTLQRAVLSTLRTQ 619
Cdd:COG4913   332 IrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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